HISZ_RALSO
ID HISZ_RALSO Reviewed; 386 AA.
AC Q8Y020;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=RSc1225;
GN ORFNames=RS02732;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC allow the feedback regulation of ATP phosphoribosyltransferase activity
CC by histidine. {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- MISCELLANEOUS: This function is generally fulfilled by the C-terminal
CC part of HisG, which is missing in some bacteria such as this one.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000255|HAMAP-Rule:MF_00125}.
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DR EMBL; AL646052; CAD14927.1; -; Genomic_DNA.
DR RefSeq; WP_011001174.1; NC_003295.1.
DR AlphaFoldDB; Q8Y020; -.
DR SMR; Q8Y020; -.
DR STRING; 267608.RSc1225; -.
DR EnsemblBacteria; CAD14927; CAD14927; RSc1225.
DR GeneID; 60500745; -.
DR KEGG; rso:RSc1225; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_4; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00125; HisZ; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR004517; HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..386
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171056"
SQ SEQUENCE 386 AA; 41184 MW; CBEEF31AB56B2FDB CRC64;
MPNWLLPESI ADVLPSEARK IEELRRRMLD LFRTYGYELV MPPMLEYIES LLSGTGHDLD
LKTFKLVDQL SGRTIGLRAD ITPQVARIDA HLLNRAGVTR LCYAGSVLHT RPSGFHVTRE
PLQIGAEIYG HAGLEADLEI QDLMLAALSA AGLADVRLDL CHVGVLAALL AQAPVAPDVQ
DELFAALASK DAPALHALTA GLPAAQRDAI NLLPSLYGGV DVLARARAQL PQLPAIGRAL
DDLATLAAHA GGAAVNIDLA DLRGYHYHSG VMFAAYVAGV PNAVARGGRY DKVGEAFGRA
RPATGFSLDL REVAGISPVQ ARAAAIHAPW SGDAKLREAI AGLRATGEIV IQSLPGHPED
LEEFAYDRQL AEEGGRWVVK PRKASA